ID A0A0L1KIT1_9EUGL Unreviewed; 697 AA.
AC A0A0L1KIT1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=asparagine--tRNA ligase {ECO:0000256|ARBA:ARBA00012816};
DE EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
DE AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029886};
GN ORFNames=XU18_3342 {ECO:0000313|EMBL:KNH05674.1}, XU18_4758
GN {ECO:0000313|EMBL:KNH03950.1};
OS Perkinsela sp. CCAP 1560/4.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Prokinetoplastina;
OC Ichthyobodonidae; Perkinsela.
OX NCBI_TaxID=1314962 {ECO:0000313|EMBL:KNH03950.1, ECO:0000313|Proteomes:UP000036983};
RN [1] {ECO:0000313|EMBL:KNH03950.1, ECO:0000313|Proteomes:UP000036983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1560/4 {ECO:0000313|EMBL:KNH03950.1};
RA Tanifuji G., David V., Flegontov P., Gerasimov E., Hashimi H.,
RA Logacheva M., Maruyama S., Onodera N., Gray M., Archibald J., Curtis B.,
RA Cenci U., Lukes J.;
RT "Draft genomes of Paramoeba pemaquidensis and its kinetoplastid
RT endosymbiont Perkinsela sp. CCAP 1560/4.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-
CC asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659,
CC Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22;
CC Evidence={ECO:0000256|ARBA:ARBA00000422};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNH03950.1}.
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DR EMBL; LFNC01000477; KNH03950.1; -; Genomic_DNA.
DR EMBL; LFNC01000235; KNH05674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L1KIT1; -.
DR EnsemblProtists; KNH03950; KNH03950; XU18_4758.
DR EnsemblProtists; KNH05674; KNH05674; XU18_3342.
DR OrthoDB; 347413at2759; -.
DR Proteomes; UP000036983; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd04323; AsnRS_cyto_like_N; 1.
DR Gene3D; 1.10.8.1290; Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1, domain 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004522; Asn-tRNA-ligase.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR007639; Gln-tRNA-synth_Ib_RNA-bd_N.
DR InterPro; IPR042558; Gln-tRNA-synth_Ib_RNA-bd_N_1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR NCBIfam; TIGR00457; asnS; 1.
DR PANTHER; PTHR22594:SF16; ASPARAGINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR Pfam; PF04558; tRNA_synt_1c_R1; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:KNH03950.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000036983}.
FT DOMAIN 375..689
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 697 AA; 78500 MW; AAFC235973C8FD48 CRC64;
MSGTPQAIAV LVEKMRSLGL DEKNATDLVK NTEKVSKLTK FFEDNDLWER TEAYSKRRMH
IYNLFMKTRE DTPKKNVLPY ILDGSIFTAL QVDEASKYVN SLESEGSFSA ERLKETCGVG
VTIENHRILD QVKQALQRIT VIPRKDVTVG QILGDIRKAG DPSMKWANQE DLRDEAAKQI
DEWRRTRSAI HIAEEKQSTL SKTENESKGK KRSECAMFSK RIAFEEFEQE SNHACRKLSL
VPEQCGQNVY VKGWVHRIRT QSKITFVVIR DGSAFVQVLL FGDDFGDLHR ETSIAVYGKV
VAEVKATGVK SSASEGNSSV CAQLPYEIHA QKFAIIGTSN GDIESVLTHE SSVDLLLDNR
HLVIRGTKTS AVLIVRSALT RAFREHFESQ EVLEVTPPTL VQTQCEGGST LFSLADYYGS
KAFLTQSSQL YLETCLPSIG DCFCIMPSYR AEKSKTRRHL SEFTHIEGEY GNITFDDLLG
KLENLVVDVL HRTVKSVGHL VALWNPASTS PGSSPYQIES FEEFLPKRPF NRMTYADAIS
FCNENGILNP ETGKDFVFGE DITDAPERQM VMKIGKPTFL IKFPASMKSF YMTKCPEEEN
LRAADPVTES VDLLLPGIGE VIGGSMRIWK YQEIMDAYAK QGLDPTNYYW YTDQRKYGGV
PHGGFGLGLE RLLVWLLALD HVRDACLYPR LMNRCAP
//
